1hb6: Difference between revisions
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|PDB= 1hb6 |SIZE=350|CAPTION= <scene name='initialview01'>1hb6</scene>, resolution 2.00Å | |PDB= 1hb6 |SIZE=350|CAPTION= <scene name='initialview01'>1hb6</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hb6 OCA], [http://www.ebi.ac.uk/pdbsum/1hb6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hb6 RCSB]</span> | |||
}} | }} | ||
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[[Category: Knudsen, J.]] | [[Category: Knudsen, J.]] | ||
[[Category: Zou, J Y.]] | [[Category: Zou, J Y.]] | ||
[[Category: acyl-coa]] | [[Category: acyl-coa]] | ||
[[Category: binding protein]] | [[Category: binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:01:28 2008'' | ||
Revision as of 21:01, 30 March 2008
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| , resolution 2.00Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF BOVINE ACYL-COA BINDING PROTEIN IN ORTHORHOMBIC CRYSTAL FORM
OverviewOverview
Acyl-CoA binding protein (ACBP) maintains a pool of fatty acyl-CoA molecules in the cell and plays a role in fatty acid metabolism. The biochemical properties of Plasmodium falciparum ACBP are described together with the 2.0 A resolution crystal structures of a P. falciparum ACBP-acyl-CoA complex and of bovine ACBP in two crystal forms. Overall, the bovine ACBP crystal structures are similar to the NMR structures published previously; however, the bovine and parasite ACBP structures are less similar. The parasite ACBP is shown to have a different ligand-binding pocket, leading to an acyl-CoA binding specificity different from that of bovine ACBP. Several non-conservative differences in residues that interact with the ligand were identified between the mammalian and parasite ACBPs. These, together with measured binding-specificity differences, suggest that there is a potential for the design of molecules that might selectively block the acyl-CoA binding site.
About this StructureAbout this Structure
1HB6 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein., van Aalten DM, Milne KG, Zou JY, Kleywegt GJ, Bergfors T, Ferguson MA, Knudsen J, Jones TA, J Mol Biol. 2001 May 25;309(1):181-92. PMID:11491287
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